Sandbox Reserved 655: Difference between revisions

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(3) Kumar, R., Sing, S., Singh, O.V. 2008. Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives. J Ind Microbiol Biotechnol. 35: 377-391.
(3) Kumar, R., Sing, S., Singh, O.V. 2008. Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives. J Ind Microbiol Biotechnol. 35: 377-391.


(4) Smith, Thomas J., and Peter E. Peterson. "The Structure of Bovine Glutamate Dehydrogenase Provides Insights into the Mechanism of Allostery." Structure 7.7 (1999): 769-782. Print.
(4) Eckert, K., Zielinski, F., Lo Leggio, L. & Schneider, E. (2002). Appl. Microbiol. Biotechnol. 60, 428–436.


(5) Smith, Emil L, et. all. "Bovine Liver Glutamate Dehydrogenase: Tentative Amino Acid Sequence; Identification of a Reactive Lysine; Nitration of a Specific Tyrosine and Loss of Allosteric Inhibition by Guanosine Triphosphate." Proceedings of the National Academy of Sciences 67.2 (1970): 724-730. Print.
(5) Sticklen, M. B. (2008). Nature (London), 9, 433–443.


(6) Godinot, Catherine, et. all. "A Rapid and Efficient New Method of Purification of Glutamate Dehydrogenase by Affinity Chromatography on GTP-Sepharose." Analytical Biochemistry 61.1 (1974): 264-270. Print.
(6) Godinot, Catherine, et. all. "A Rapid and Efficient New Method of Purification of Glutamate Dehydrogenase by Affinity Chromatography on GTP-Sepharose." Analytical Biochemistry 61.1 (1974): 264-270. Print.
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